Evidence map›Paper›PMID 20440001›Full record

ArticleThe Journal of cell biology2010

Lack of Apobec2-related proteins causes a dystrophic muscle phenotype in zebrafish embryos.

Christelle Etard, Urmas Roostalu, Uwe Strähle

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 57 citations in OpenAlex.

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  11. Apobec2 deficiency causes mitochondrial defects and mitophagy in skeletal muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christelle EtardInstitute of Toxicology and Genetics, Forschungszentrum Karlsruhe in the Helmholtz Association, Karlsruhe Institute of Technology, Karlsruhe, Germany.
Urmas Roostalu
Uwe Strähle
Karlsruhe Institute of Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chaperones Unc45b and Hsp90a are essential for folding of myosin in organisms ranging from worms to humans. We show here that zebrafish Unc45b, but not Hsp90a, binds to the putative cytidine deaminase Apobec2 (Apo2) in an interaction that requires the Unc45/Cro1p/She4p-related (UCS) and central domains of Unc45b. Morpholino oligonucleotide-mediated knockdown of the two related proteins Apo2a and Apo2b causes a dystrophic phenotype in the zebrafish skeletal musculature and impairs heart function. These phenotypic traits are shared with mutants of unc45b, but not with hsp90a mutants. Apo2a and -2b act nonredundantly and bind to each other in vitro, which suggests a heteromeric functional complex. Our results demonstrate that Unc45b and Apo2 proteins act in a Hsp90a-independent pathway that is required for integrity of the myosepta and myofiber attachment. Because the only known function of Unc45b is that of a chaperone, Apo2 proteins may be clients of Unc45b but other yet unidentified processes cannot be excluded.

Indexed as

PhenotypeAnimalsCytidine DeaminaseEmbryo, NonmammalianHSP90 Heat-Shock ProteinsMolecular ChaperonesMuscle ProteinsMuscle, SkeletalType C PhospholipasesZebrafishZebrafish ProteinsCytidine DeaminaseHSP90 Heat-Shock ProteinsMolecular ChaperonesMuscle Proteinsplcb3 protein, zebrafishType C PhospholipasesUnc45b protein, zebrafishZebrafish Proteins

Identifiers

PMID20440001
PMCPMC2867308
OpenAlexW2141884494

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.